α - 1-巯基蛋白酶抑制剂的纯化、鉴定及其与激肽和无片段1.2高分子量激肽原的同源性。

I Ohkubo, C Namikawa, S Higashiyama, M Sasaki, O Minowa, Y Mizuno, H Shiokawa
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引用次数: 19

摘要

1. α 1-巯基蛋白酶抑制剂(α 1 TPI)是从过时的人血浆中纯化出来的,分子量为83,000,由重链和轻链通过二硫键连接在一起组成。2. 氨基酸组成、轻链氨基末端序列、重链和轻链羧基末端序列数据表明,α 1 TPI与无激肽和无片段1.2的HMW激肽原相同。3.纯化后的人纤溶蛋白衍生物与HMW激肽原和不含HMW激肽原的α 1 TPI具有相同的分子量(Mr 83,000)、相同的亚基结构(重链和轻链)和相同的抑制能力。这表明α 1 TPI可能是由HMW激肽原通过纤溶酶产生的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Purification and characterization of alpha 1-thiol proteinase inhibitor and its identity with kinin- and fragment 1.2-free high molecular weight kininogen.

1. alpha 1-Thiol proteinase inhibitor (alpha 1 TPI) purified from outdated human plasma was a glycoprotein with Mr 83,000 and was composed of heavy and light chains held together with a disulfide bond. 2. The data on amino acid composition, amino terminal sequence of the light chain and carboxyl terminal sequences of the heavy and light chains indicate that alpha 1 TPI is identical with kinin- and fragment 1.2-free HMW kininogen. 3. Purified human plasmin generated a derivative having the same molecular weight (Mr 83,000), same subunit structure (heavy and light chains) and same inhibitory capacity as alpha 1 TPI from HMW kininogen and kinin-free HMW kininogen. This indicated the possibility that alpha 1 TPI is derived from HMW kininogen by plasmin.

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